CA2327524C - Method of controlling cleavage by ompt protease - Google Patents

Method of controlling cleavage by ompt protease Download PDF

Info

Publication number: CA2327524C
Authority: CA; Canada
Prior art keywords: amino acid; ompt protease; cleavage; site; fusion protein
Prior art date: 1999-03-04
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.): Expired - Fee Related

Application number

CA002327524A

Other languages

English (en)

French (fr)

Other versions

CA2327524A1 (en

Inventor

Kazuaki Okuno

Masayuki Yabuta

Kazuhiro Ohsuye

Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)

Asubio Pharma Co Ltd

Original Assignee

Asubio Pharma Co Ltd

Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)

1999-03-04

Filing date

2000-03-03

Publication date

2010-02-02

2000-03-03 Application filed by Asubio Pharma Co Ltd filed Critical Asubio Pharma Co Ltd

2000-09-08 Publication of CA2327524A1 publication Critical patent/CA2327524A1/en

2010-02-02 Application granted granted Critical

2010-02-02 Publication of CA2327524C publication Critical patent/CA2327524C/en

2020-03-03 Anticipated expiration legal-status Critical

Status Expired - Fee Related legal-status Critical Current

Links

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IZTQOLKUZKXIRV-YRVFCXMDSA-N sincalide Chemical compound C([C@@H](C(=O)N[C@@H](CCSC)C(=O)NCC(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC=1C=CC=CC=1)C(N)=O)NC(=O)[C@@H](N)CC(O)=O)C1=CC=C(OS(O)(=O)=O)C=C1 IZTQOLKUZKXIRV-YRVFCXMDSA-N 0.000 description 1
239000011684 sodium molybdate Substances 0.000 description 1
235000015393 sodium molybdate Nutrition 0.000 description 1
TVXXNOYZHKPKGW-UHFFFAOYSA-N sodium molybdate (anhydrous) Chemical compound [Na+].[Na+].[O-][Mo]([O-])(=O)=O TVXXNOYZHKPKGW-UHFFFAOYSA-N 0.000 description 1
NHXLMOGPVYXJNR-ATOGVRKGSA-N somatostatin Chemical compound C([C@H]1C(=O)N[C@H](C(N[C@@H](CO)C(=O)N[C@@H](CSSC[C@@H](C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@@H](CC=2C3=CC=CC=C3NC=2)C(=O)N[C@@H](CCCCN)C(=O)N[C@H](C(=O)N1)[C@@H](C)O)NC(=O)CNC(=O)[C@H](C)N)C(O)=O)=O)[C@H](O)C)C1=CC=CC=C1 NHXLMOGPVYXJNR-ATOGVRKGSA-N 0.000 description 1
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235000008521 threonine Nutrition 0.000 description 1
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LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
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SJMPVWVIVWEWJK-AXEIBBKLSA-N uroguanylin Chemical compound SC[C@@H](C(O)=O)NC(=O)CNC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CS)NC(=O)[C@H](C)NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H]([C@@H](C)CC)NC(=O)[C@H](CS)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CS)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@@H](N)CCC(N)=O SJMPVWVIVWEWJK-AXEIBBKLSA-N 0.000 description 1
108010073969 valyllysine Proteins 0.000 description 1
229960003726 vasopressin Drugs 0.000 description 1
230000003612 virological effect Effects 0.000 description 1
238000005406 washing Methods 0.000 description 1
229910000368 zinc sulfate Inorganic materials 0.000 description 1
NWONKYPBYAMBJT-UHFFFAOYSA-L zinc sulfate Chemical compound [Zn+2].[O-]S([O-])(=O)=O NWONKYPBYAMBJT-UHFFFAOYSA-L 0.000 description 1
239000011686 zinc sulphate Substances 0.000 description 1
235000009529 zinc sulphate Nutrition 0.000 description 1
NXSIJWJXMWBCBX-NWKQFZAZSA-N α-endorphin Chemical compound C([C@@H](C(=O)N[C@@H](CCSC)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H]([C@@H](C)O)C(O)=O)NC(=O)CNC(=O)CNC(=O)[C@@H](N)CC=1C=CC(O)=CC=1)C1=CC=CC=C1 NXSIJWJXMWBCBX-NWKQFZAZSA-N 0.000 description 1

Classifications

- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
- C12P21/02—Preparation of peptides or proteins having a known sequence of two or more amino acids, e.g. glutathione
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/575—Hormones
- C07K14/585—Calcitonins
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/575—Hormones
- C07K14/58—Atrial natriuretic factor complex; Atriopeptin; Atrial natriuretic peptide [ANP]; Cardionatrin; Cardiodilatin
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/575—Hormones
- C07K14/605—Glucagons
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
- C12N15/62—DNA sequences coding for fusion proteins
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/50—Fusion polypeptide containing protease site
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/70—Fusion polypeptide containing domain for protein-protein interaction
- C07K2319/74—Fusion polypeptide containing domain for protein-protein interaction containing a fusion for binding to a cell surface receptor
- C07K2319/75—Fusion polypeptide containing domain for protein-protein interaction containing a fusion for binding to a cell surface receptor containing a fusion for activation of a cell surface receptor, e.g. thrombopoeitin, NPY and other peptide hormones

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Health & Medical Sciences (AREA)
Life Sciences & Earth Sciences (AREA)
Chemical & Material Sciences (AREA)
Genetics & Genomics (AREA)
Organic Chemistry (AREA)
Engineering & Computer Science (AREA)
Zoology (AREA)
Molecular Biology (AREA)
General Health & Medical Sciences (AREA)
Biochemistry (AREA)
Wood Science & Technology (AREA)
Biophysics (AREA)
Biomedical Technology (AREA)
General Engineering & Computer Science (AREA)
Bioinformatics & Cheminformatics (AREA)
Biotechnology (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Gastroenterology & Hepatology (AREA)
Medicinal Chemistry (AREA)
Endocrinology (AREA)
Toxicology (AREA)
Microbiology (AREA)
Physics & Mathematics (AREA)
Plant Pathology (AREA)
Cardiology (AREA)
Chemical Kinetics & Catalysis (AREA)
General Chemical & Material Sciences (AREA)
Peptides Or Proteins (AREA)
Micro-Organisms Or Cultivation Processes Thereof (AREA)
Preparation Of Compounds By Using Micro-Organisms (AREA)
Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Enzymes And Modification Thereof (AREA)

CA002327524A 1999-03-04 2000-03-03 Method of controlling cleavage by ompt protease Expired - Fee Related CA2327524C (en)

Applications Claiming Priority (3)

Application Number	Priority Date	Filing Date	Title
JP11/57731		1999-03-04
JP5773199		1999-03-04
PCT/JP2000/001309 WO2000052193A1 (fr)	1999-03-04	2000-03-03	Procede de controle de clivage par la protease de l'ompt

Publications (2)

Publication Number	Publication Date
CA2327524A1 CA2327524A1 (en)	2000-09-08
CA2327524C true CA2327524C (en)	2010-02-02

Family

ID=13064080

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
CA002327524A Expired - Fee Related CA2327524C (en)	1999-03-04	2000-03-03	Method of controlling cleavage by ompt protease

Country Status (12)

Country	Link
US (1)	US7344856B1 (de)
EP (1)	EP1076097B1 (de)
JP (1)	JP4471501B2 (de)
KR (1)	KR100916169B1 (de)
CN (1)	CN100445394C (de)
AT (1)	ATE414164T1 (de)
AU (1)	AU758633B2 (de)
CA (1)	CA2327524C (de)
DE (1)	DE60040771D1 (de)
ES (1)	ES2316352T3 (de)
IL (1)	IL139338A0 (de)
WO (1)	WO2000052193A1 (de)

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WO2003084983A1 (en)	2002-04-11	2003-10-16	Daiichi Suntory Pharma Co., Ltd.	Process for producing modified peptide
AU2004276687B2 (en) *	2003-09-30	2011-07-14	Asubio Pharma Co., Ltd.	Method of cleaving polypeptide by using OmpT protease mutant
US8586294B2 (en)	2004-05-18	2013-11-19	The Board Of Trustees Of The Leland Stanford Junior University	Detection of protein translocation by beta-galactosidase reporter fragment complementation
US8030447B2 (en)	2006-09-20	2011-10-04	The Board Of Regents Of The University Of Texas System	Substrate peptide sequences for plague plasminogen activator and uses thereof
CN102707054B (zh) *	2012-06-18	2014-11-05	黑龙江八一农垦大学	大肠埃希氏菌OmpT抗体间接ELISA检测方法
JP6421122B2 (ja)	2012-10-12	2018-11-07	ストロバイオファーマ，インコーポレイテッド	改善された発現のための、細菌抽出物中の選択タンパク質のタンパク質分解不活性化
EP3852810A4 (de) *	2018-09-19	2022-12-07	Georgia Tech Research Corporation	Biologische bits als berechenbare elemente in lebenden systemen

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DE69937272T2 (de) *	1998-01-30	2008-07-10	Asubio Pharma Co., Ltd.	Verfahren zur herstellung eines peptids mittels eines hilfspeptids

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IL139338A0 (en)	2001-11-25
AU2828800A (en)	2000-09-21
CN1302337A (zh)	2001-07-04
CN100445394C (zh)	2008-12-24
KR20010043333A (ko)	2001-05-25
US7344856B1 (en)	2008-03-18
CA2327524A1 (en)	2000-09-08
ATE414164T1 (de)	2008-11-15
AU758633B2 (en)	2003-03-27
KR100916169B1 (ko)	2009-09-08
EP1076097A1 (de)	2001-02-14
EP1076097B1 (de)	2008-11-12
DE60040771D1 (de)	2008-12-24
JP4471501B2 (ja)	2010-06-02
EP1076097A4 (de)	2003-02-05
WO2000052193A1 (fr)	2000-09-08
ES2316352T3 (es)	2009-04-16

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